Evolutionary insights into premetazoan functions of the neuronal protein homer
Open accessAbstract
Reconstructing the evolution and ancestral functions of synaptic proteins promises to shed light on how neurons first evolved. The postsynaptic density (PSD) protein Homer scaffolds membrane receptors and regulates Ca(2+) signaling in diverse metazoan cell types (including neurons and muscle cells), yet its ancestry and core functions are poorly understood. We find that the protein domain organization and essential biochemical properties of metazoan Homer proteins, including their ability to tetramerize, are conserved in the choanoflagellate Salpingoeca rosetta, one of the closest living relatives of metazoans. Unlike in neurons, Homer localizes to the nucleoplasm in S. rosetta and interacts directly with Flotillin, a protein more commonly associated with cell membranes. Surprisingly, we found that the Homer/Flotillin interaction and its localization to the nucleus are conserved in metazoan astrocytes. These findings suggest that Homer originally interacted with Flotillin in the nucleus of the last common ancestor of metazoans and choanoflagellates and was later co-opted to function as a membrane receptor scaffold in the PSD.
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Of the 74 protein components of the mammalian nervous system listed by Burkhardt et al., only three lack homologs in other phyla.
“of the 74 protein components of the mammalian nervous system listed by Burkhardt et al. [33], only three (SynCam, Piccolo and Bassoon) lack homologs in other phyla”
From Back to the Basics: Cnidarians Start to Fire (2017) · cites this paper as [33]
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- Authors
- Burkhardt, P., Grønborg, M., McDonald, K., Sulur, T., Wang, Q., & King, N.
- Affiliations
- Howard Hughes Medical Institute (US)
- Novo Nordisk (Denmark) (DK)
- University of California, Berkeley (US)
- QB3 (US)
- Corresponding author
- King, Nicole
- Venue
- Molecular Biology and Evolution
- Publisher
- Oxford University Press (OUP)
- Published
- 2014-06-03
- Volume
- 31
- Issue
- 9
- Pages
- 2342-2355
- ISSN
- 0737-4038 (ISSN-L)
- 1537-1719
- PMC
- PMC4137706
- OpenAlex
- W2160586365
- Cited by
- 56
- References
- 67
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 5 · 2023: 2 · 2022: 4 · 2021: 3 · 2020: 6 · 2019: 6 · 2018: 4 · 2017: 6 · 2016: 5 · 2015: 7 · 2014: 2
- FWCI
- 3.05
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc
- Locations
- Molecular Biology and Evolution (publishedVersion, cc-by-nc)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- eScholarship (California Digital Library) (submittedVersion, cc-by-nc)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- Deutsche Forschungsgemeinschaft
- National Institutes of Health
- National Institute of General Medical Sciences (GM089977, R01GM089977)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Physical Sciences › Earth and Planetary Sciences › Paleontology › Marine Invertebrate Physiology and Ecology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
- Keywords
- Homer proteins, synaptic proteins, postsynaptic density, choanoflagellates, Salpingoeca rosetta, flotillin, nuclear localization, tetramerization, protein domain organization, astrocytes, calcium signaling, ancestral function, animal evolution
- MeSH terms
- Homer Scaffolding Proteins, Animals, Astrocytes, Carrier Proteins, Cell Nucleus, Membrane Proteins, Phylogeny, Evolution, Molecular, Rats, Choanoflagellata
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